Time-Resolved X-ray Absorption Determination of Structural Changes following Photoinduced Electron Transfer within Bis-porphyrin Heme Protein Models

1999 ◽  
Vol 103 (16) ◽  
pp. 3270-3274 ◽  
Author(s):  
Lin X. Chen ◽  
Peter L. Lee ◽  
David Gosztola ◽  
Walter A. Svec ◽  
Pedro A. Montano ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photoinduced Electron Transfer ◽  
Structural Changes ◽  
Heme Protein ◽  
Time Resolved ◽  
X Ray ◽  
Absorption Determination ◽  
Protein Models ◽  
X Ray Absorption

K-Capture Spectroscopy. Iron-55 X-Ray Absorption Determination of Sulfur in Hydrocarbons

1954 ◽  
Vol 26 (12) ◽  
pp. 1889-1893 ◽  
Author(s):  
H. K. Hughes ◽  
J. W. Wilczewski
Keyword(s):  
X Ray ◽  
Absorption Determination ◽  
X Ray Absorption

scholarly journals Preparing for SwissFEL: Exploring the limits of time-resolved X-ray spectroscopy

2014 ◽  
Vol 70 (a1) ◽  
pp. C129-C129
Author(s):  
Chris Milne ◽  
Jakub Szlachetko ◽  
Tom Penfold ◽  
Majed Chergui ◽  
Rafael Abela
Keyword(s):  
Structural Changes ◽  
Probe Laser ◽  
Time Resolved ◽  
X Ray ◽  
Ligand Rebinding ◽  
Femtosecond Regime ◽  
Under Construction ◽  
Paul Scherrer ◽  
Pulse Energies ◽  
X Ray Absorption

Using x-ray absorption spectroscopy (XAS) and x-ray emission spectroscopy (XES) to probe laser-excited samples we can obtain excited-state structural and electronic dynamical information not available through other techniques.[1] One of the restrictions of most synchrotron-based implementations of this technique is the three-orders of magnitude mismatch between x-ray and laser repetition rates (MHz Vs. kHz). By using a laser capable of generating significant pulse energies at MHz repetition rates we can eliminate this discrepancy, thus greatly reducing measurement times and enhancing achievable signal-to-noise ratios.[2] Several examples that demonstrate the strength of this technique will be presented, including probing the electron relaxation in photoexcited TiO2 nanoparticles in solution and resolving the dynamical structural changes associated with ligand rebinding in the protein myoglobin under physiological conditions. The ability to extend these types of measurements into the femtosecond regime at Experimental Station A[3] at the SwissFEL hard X-ray free electron laser, which is under construction at the Paul Scherrer Institute (Villigen, Switzerland), will be discussed.

scholarly journals Elucidating light-induced charge accumulation in an artificial analogue of methane monooxygenase enzymes using time-resolved X-ray absorption spectroscopy

2017 ◽  
Vol 53 (18) ◽  
pp. 2725-2728 ◽  
Author(s):  
Dooshaye Moonshiram ◽  
Antonio Picón ◽  
Alvaro Vazquez-Mayagoitia ◽  
Xiaoyi Zhang ◽  
Ming-Feng Tu ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Charge Accumulation ◽  
Time Resolved ◽  
X Ray ◽  
Transfer Processes ◽  
System P ◽  
Photocatalytic System ◽  
Induced Charge ◽  
Electron Transfer Processes ◽  
X Ray Absorption

Probing the light-induced two electron transfer processes at a diiron(iii,iii) multimolecular photocatalytic system.

A new experimental setup for time- and laterally-resolved X-ray absorption fine structure spectroscopy in a ‘single shot’

2019 ◽  
Vol 34 (1) ◽  
pp. 239-246 ◽  
Author(s):  
A. Kulow ◽  
S. Witte ◽  
S. Beyer ◽  
A. Guilherme Buzanich ◽  
M. Radtke ◽  
...  
Keyword(s):  
Fine Structure ◽  
Structural Changes ◽  
Chemical Compounds ◽  
Experimental Setup ◽  
Single Shot ◽  
Time Resolved ◽  
X Ray ◽  
Absorption Fine ◽  
X Ray Absorption

A new, simple and adjustable setup allows scanning-free XAS for time-resolved studies of structural changes in chemical compounds.

scholarly journals Synchrotron ultrafast techniques for photoactive transition metal complexes

2013 ◽  
Vol 371 (1995) ◽  
pp. 20120132 ◽  
Author(s):  
Elisa Borfecchia ◽  
Claudio Garino ◽  
Luca Salassa ◽  
Carlo Lamberti
Keyword(s):  
Transition Metal ◽  
Metal Complexes ◽  
Transition Metal Complexes ◽  
Structural Changes ◽  
Time Resolved ◽  
X Ray ◽  
Use Of Time ◽  
Wide Range ◽  
Analysis Strategies ◽  
X Ray Absorption

In the last decade, the use of time-resolved X-ray techniques has revealed the structure of light-generated transient species for a wide range of samples, from small organic molecules to proteins. Time resolutions of the order of 100 ps are typically reached, allowing one to monitor thermally equilibrated excited states and capture their structure as a function of time. This review aims at providing a general overview of the application of time-resolved X-ray solution scattering (TR-XSS) and time-resolved X-ray absorption spectroscopy (TR-XAS), the two techniques prevalently employed in the investigation of light-triggered structural changes of transition metal complexes. In particular, we herein describe the fundamental physical principles for static XSS and XAS and illustrate the theory of time-resolved XSS and XAS together with data acquisition and analysis strategies. Selected pioneering examples of photoactive transition metal complexes studied by TR-XSS and TR-XAS are discussed in depth.

scholarly journals Anisotropy enhanced X-ray scattering from solvated transition metal complexes

2018 ◽  
Vol 25 (2) ◽  
pp. 306-315 ◽  
Author(s):  
Elisa Biasin ◽  
Tim B. van Driel ◽  
Gianluca Levi ◽  
Mads G. Laursen ◽  
Asmus O. Dohn ◽  
...  
Keyword(s):  
Structural Changes ◽  
Platinum Complex ◽  
Anisotropic Scattering ◽  
Isotropic Scattering ◽  
Time Resolved ◽  
Instrument Response Function ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Time-resolved X-ray scattering patterns from photoexcited molecules in solution are in many cases anisotropic at the ultrafast time scales accessible at X-ray free-electron lasers (XFELs). This anisotropy arises from the interaction of a linearly polarized UV–Vis pump laser pulse with the sample, which induces anisotropic structural changes that can be captured by femtosecond X-ray pulses. In this work, a method for quantitative analysis of the anisotropic scattering signal arising from an ensemble of molecules is described, and it is demonstrated how its use can enhance the structural sensitivity of the time-resolved X-ray scattering experiment. This method is applied on time-resolved X-ray scattering patterns measured upon photoexcitation of a solvated di-platinum complex at an XFEL, and the key parameters involved are explored. It is shown that a combined analysis of the anisotropic and isotropic difference scattering signals in this experiment allows a more precise determination of the main photoinduced structural change in the solute,i.e.the change in Pt—Pt bond length, and yields more information on the excitation channels than the analysis of the isotropic scattering only. Finally, it is discussed how the anisotropic transient response of the solvent can enable the determination of key experimental parameters such as the instrument response function.

Upgrade of laser pump time-resolved X-ray probes in Beijing synchrotron

2019 ◽  
Vol 26 (6) ◽  
pp. 2075-2080
Author(s):  
Can Yu ◽  
Yan Zhang ◽  
Ge Lei ◽  
Hao Wang ◽  
Yu-hang Wang ◽  
...  
Keyword(s):  
Thin Film ◽  
Structural Changes ◽  
High Efficiency ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Laser Pump ◽  
Acquisition Scheme ◽  
First Time ◽  
X Ray Absorption

The upgrade of the laser pump time-resolved X-ray probes, namely time-resolved X-ray absorption spectroscopy (TR-XAS) and X-ray diffraction (TR-XRD), implemented at the Beijing Synchrotron Radiation Facility, is described. The improvements include a superbunch fill, a high-efficiency fluorescence collection, an efficient spatial overlap protocol and a new data-acquisition scheme. After upgrade, the adequate TR-XAS signal is now obtained in a 0.3 mM solution, compared with a 6 mM solution in our previous report. Furthermore, to extend application in photophysics, the TR-XAS probe is applied on SrCoO2.5 thin film. And for the first time, TR-XAS is combined with TR-XRD to simultaneously detect the kinetic trace of structural changes in thin film.

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